Research workbench
Crystal structure of asfvpolx in complex with DNA enzyme.
Analyse Crystal structure of asfvpolx in complex with DNA enzyme. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5XM9
- Type
- protein + DNA
- Length
- 814 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Repair DNA polymerase X; DNA (36-mer); DNA (23-mer)
- EC
- 2.7.7.7
- UniProt
- P42494
- Pockets
- 15 · best druggability 0.69
Structure
x-ray diffraction · 3 distinct chains · 32% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Repair DNA polymerase X (EC 2.7.7.7) | protein | 174 | 32% helix, 32% strand | P42494 |
| E, G | DNA (36-mer) | dna | 36 | — | — |
| F, H | DNA (23-mer) | dna | 23 | — | — |
Pockets
15 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 51 | 0.69 | 0.98 | 18 | empty |
| 2 | 56 | 0.68 | 0.96 | 18 | empty |
| 3 | 288 | 0.56 | 0.77 | 37 | empty |
| 4 | 191 | 0.50 | 0.77 | 24 | empty |
| 5 | 306 | 0.48 | 0.72 | 28 | empty |
Interfaces
14 interfaces between chains.
- G–H · 1175 Ų buried · 110 hydrogen bonds · nucleic-nucleic
- E–F · 1166 Ų buried · 105 hydrogen bonds · nucleic-nucleic
- A–E · 677 Ų buried · 15 hydrogen bonds · protein-nucleic
- C–G · 595 Ų buried · 13 hydrogen bonds · protein-nucleic
- B–F · 569 Ų buried · 18 hydrogen bonds · protein-nucleic
Compared structures
- 5XM9 · Crystal structure of AsfvPolX in complex with DNA enzyme. · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P42494
- Elsewhere: RCSB PDB 5XM9 · PDBe 5XM9 · UniProt P42494
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.